HXKG_ASPNG
ID HXKG_ASPNG Reviewed; 495 AA.
AC Q92407;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glucokinase;
DE EC=2.7.1.2 {ECO:0000269|PubMed:8856049};
DE AltName: Full=Glucose kinase;
DE Short=GLK;
DE AltName: Full=Hexokinase glkA {ECO:0000305};
DE EC=2.7.1.1 {ECO:0000269|PubMed:8856049};
GN Name=glkA;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=8856049; DOI=10.1111/j.1432-1033.1996.0518h.x;
RA Panneman H., Ruijter G.J.G., van den Broeck H.C., Driever E.T.M.,
RA Visser J.;
RT "Cloning and biochemical characterisation of an Aspergillus niger
RT glucokinase. Evidence for the presence of separate glucokinase and
RT hexokinase enzymes.";
RL Eur. J. Biochem. 240:518-525(1996).
CC -!- FUNCTION: The enzyme has great affinity for glucose. Mannose, 2-
CC deoxyglucose and glucosamine can serve as substrates.
CC {ECO:0000269|PubMed:8856049}.
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:0000269|PubMed:8856049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:8856049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:8856049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:8856049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:8856049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000269|PubMed:8856049};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+);
CC Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:8856049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10949;
CC Evidence={ECO:0000269|PubMed:8856049};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Activity is relatively constant from pH 7.5 to 9.0. Below pH 7.5,
CC activity decreases with pH.;
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:8856049}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:8856049}.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; X99626; CAA67949.1; -; Genomic_DNA.
DR PIR; S74210; S74210.
DR AlphaFoldDB; Q92407; -.
DR SMR; Q92407; -.
DR STRING; 5061.CADANGAP00010094; -.
DR PRIDE; Q92407; -.
DR VEuPathDB; FungiDB:An12g08610; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1143262; -.
DR VEuPathDB; FungiDB:ATCC64974_34790; -.
DR VEuPathDB; FungiDB:M747DRAFT_15974; -.
DR eggNOG; KOG1369; Eukaryota.
DR BRENDA; 2.7.1.2; 518.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0047931; F:glucosamine kinase activity; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0019158; F:mannokinase activity; IEA:RHEA.
DR GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006013; P:mannose metabolic process; IEA:UniProt.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..495
FT /note="Glucokinase"
FT /id="PRO_0000197611"
FT DOMAIN 3..483
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 57..206
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 149..175
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 207..472
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 472..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 54537 MW; 02C94EF07D1809F8 CRC64;
MSSALLDEAA RIARQFDYPA AEVQRGVTEY IREIDEGLSK EHTTLSQIPT YVTAVPNGTE
KGLYLAVDLG GTNFRVCSID LHGDTTFSLT QSKIMIPRET MASGTAKDLF LFLARQIESF
LRIHHNDHFE AHLRRRNEKN GNCEEDLFDL GFTFSFPVRQ LGINKGTLIR WTKGFNIPDA
VGKDVCALLQ NAIDDLGLPV RVAALVNDTV GTLMARSYTS PGETGTFLGA IFGTGTNGAY
VEKLDRITKL QTIEHSEYDK TTGEMIINAE WGSFDNHLSV LPNTIYDQQL DADSNNPGIQ
MFEKRVSGMF LGEILRRVML DMQRNESLGF LRAGGASTVS VPQESSLYRQ WGIDTSLLSL
VEADKTENME QIKVALKDHL KIERPTTDDC KAIQTVVHAI GKRAARLSAV PLAAILLSTG
KLQKDDLVDI GVDGSLVEFY PNFEGYMRDA LREVPEVGEA GNKKIRIGIS KDGSGVGAAL
IALVASKEET RRKSQ
