HXK_BRUMA
ID HXK_BRUMA Reviewed; 572 AA.
AC A0A0K0JFP3; Q56VN6;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Hexokinase {ECO:0000303|PubMed:18499511};
DE Short=BmHK {ECO:0000303|PubMed:18499511};
DE EC=2.7.1.1 {ECO:0000269|PubMed:18499511};
GN ORFNames=Bm4678 {ECO:0000312|EMBL:CRZ23240.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279;
RN [1] {ECO:0000312|EMBL:AAR13363.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=18499511; DOI=10.1016/j.parint.2008.03.004;
RA Singh A.R., Joshi S., Arya R., Kayastha A.M., Srivastava K.K.,
RA Tripathi L.M., Saxena J.K.;
RT "Molecular cloning and characterization of Brugia malayi hexokinase.";
RL Parasitol. Int. 57:354-361(2008).
RN [2] {ECO:0000312|EMBL:CRZ23240.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FR3 {ECO:0000312|EMBL:CRZ23240.1};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K.S., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
CC -!- FUNCTION: Active against glucose, fructose, mannose, maltose and
CC galactose. {ECO:0000269|PubMed:18499511}.
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:0000255|PROSITE-ProRule:PRU01084,
CC ECO:0000269|PubMed:18499511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:18499511};
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:18499511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC Evidence={ECO:0000269|PubMed:18499511};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:18499511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000269|PubMed:18499511};
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=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:18499511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:18499511};
CC -!- ACTIVITY REGULATION: Activated by glucose-6-phosphate. Inhibited by N-
CC acetylglucosamine, glucosamine, mannoheptulose and ADP.
CC {ECO:0000269|PubMed:18499511}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.035 mM for glucose {ECO:0000269|PubMed:18499511};
CC KM=75 mM for fructose {ECO:0000269|PubMed:18499511};
CC KM=1.09 mM for ATP {ECO:0000269|PubMed:18499511};
CC pH dependence:
CC Optimum pH is 8.4. {ECO:0000269|PubMed:18499511};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000269|PubMed:18499511}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000269|PubMed:18499511}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255,
CC ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000255|RuleBase:RU362007}.
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DR EMBL; AY341346; AAR13363.1; -; mRNA.
DR EMBL; LN856840; CRZ23240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0JFP3; -.
DR SMR; A0A0K0JFP3; -.
DR STRING; 6279.A0A0K0JFP3; -.
DR EnsemblMetazoa; Bm4678.1; Bm4678.1; WBGene00224939.
DR WBParaSite; Bm4678.1; Bm4678.1; WBGene00224939.
DR WormBase; Bm4678; BM38607; WBGene00224939; Bma-hxk-2.
DR BRENDA; 2.7.1.1; 997.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR GO; GO:0004340; F:glucokinase 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:0019318; P:hexose metabolic process; IDA:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
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; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..572
FT /note="Hexokinase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437173"
FT DOMAIN 49..492
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 105..237
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 238..481
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 116..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 116..120
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 185..186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 185
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 202..203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 239
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 263
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 266
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 336..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 373..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 446..448
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 448..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 483
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT CONFLICT 68
FT /note="T -> S (in Ref. 1; AAR13363)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="G -> S (in Ref. 1; AAR13363)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..509
FT /note="Missing (in Ref. 1; AAR13363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 64043 MW; C2675B140514684B CRC64;
MLGLLTITSV FRNWRNSLQR KEDYDECHMR GINNENEISG KSEKNFKLDE PPISLETVMA
EFKLSNETLR RMMAHMSRNM DKGLEGGPEN STISMLPSFV PELPNGTEEG RFIAMDLGGT
NLRVMLMDIK PGEELKTEQF NTRIPNWAMR GTGEQLFDYI TKCLAEFLIE KGIENDGLPV
GFTFSYPCDQ KSLRSATLLR WTKGFETTGV VGEDVVELLE QSIARRGDIK VEVVALINDT
VGTMVAAAHE SGGECHIGVI IATGTNASYM EDTSKIKYGL SKAIAAYNYP EMIIDTEWGG
FGDRSEADYI LTQYDKIVDS RSEHPGVNTF DKLVGGKCMG EVVRVVLEKL TRARVLFNGK
GSDALFQQDS FPTKYISEIL RDESGSYVHT RDILGELGID HYSFSDMLLL REVCVVVSRR
SANLGAAAIA CVLNRVRKQN MVVGIDGSTY KYHPFFDFWV HDKLKELVDP GLKFKLLQTA
DGSGKGAALI TAIVARLKKR NLKQQQQQQQ QQQQHVTMVE QNVVEQIAET KGSREQFMNG
NQKINLVTND IPIYDSFNGD IENGVIHLST DH
