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 31-JUL-2019, entry version 17. 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 {ECO:0000312|WBParaSite:Bm4678}; 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., RA Allen J.E., Delcher A.L., Guiliano D.B., Miranda-Saavedra D., RA Angiuoli S.V., Creasy T., Amedeo P., Haas B., El-Sayed N.M., RA Wortman J.R., Feldblyum T., Tallon L., Schatz M., Shumway M., Koo H., RA Salzberg S.L., Schobel S., Pertea M., Pop M., White O., Barton G.J., RA Carlow C.K.S., Crawford M.J., Daub J., Dimmic M.W., Estes C.F., RA Foster J.M., Ganatra M., Gregory W.F., Johnson N.M., Jin J., RA Komuniecki R., Korf I., Kumar S., Laney S., Li B.-W., Li W., RA 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; CC EC=2.7.1.1; 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; CC EC=2.7.1.1; 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; CC EC=2.7.1.1; 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; CC EC=2.7.1.1; 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 CC by N-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. CC {ECO:0000255|PROSITE-ProRule:PRU01084, CC ECO:0000255|RuleBase:RU362007, ECO:0000255|SAAS:SAAS00541710}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY341346; AAR13363.1; -; mRNA. DR EMBL; LN856840; CRZ23240.1; -; Genomic_DNA. DR SMR; A0A0K0JFP3; -. DR EnsemblMetazoa; Bm4678; Bm4678; WBGene00224939. DR WBParaSite; Bm4678; Bm4678; WBGene00224939. DR BRENDA; 2.7.1.1; 997. DR UniPathway; UPA00109; UER00180. DR UniPathway; UPA00242; -. DR Proteomes; UP000006672; Unassembled WGS sequence. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005536; F:glucose binding; IEA:InterPro. DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC. DR GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR GO; GO:0019318; P:hexose metabolic process; IDA:UniProtKB. 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 PROSITE; PS51748; HEXOKINASE_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 572 Hexokinase. {ECO:0000305}. FT /FTId=PRO_0000437173. FT DOMAIN 49 492 Hexokinase. {ECO:0000255|PROSITE- FT ProRule:PRU01084}. FT NP_BIND 116 121 ATP. {ECO:0000250|UniProtKB:P19367}. FT NP_BIND 336 337 ATP. {ECO:0000250|UniProtKB:P19367}. FT NP_BIND 373 377 ATP. {ECO:0000250|UniProtKB:P19367}. FT NP_BIND 448 452 ATP. {ECO:0000250|UniProtKB:P19367}. FT REGION 105 237 Hexokinase small subdomain. FT {ECO:0000255|PROSITE-ProRule:PRU01084}. FT REGION 116 120 Glucose-6-phosphate binding. FT {ECO:0000250|UniProtKB:P19367}. FT REGION 185 186 Substrate binding. FT {ECO:0000250|UniProtKB:P19367}. FT REGION 202 203 Substrate binding. FT {ECO:0000250|UniProtKB:P19367}. FT REGION 238 481 Hexokinase large subdomain. FT {ECO:0000255|PROSITE-ProRule:PRU01084}. FT REGION 238 239 Substrate binding. FT {ECO:0000250|UniProtKB:P19367}. FT REGION 446 448 Glucose-6-phosphate binding. FT {ECO:0000250|UniProtKB:P19367}. FT COMPBIAS 504 526 Gln-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00006}. FT BINDING 185 185 Glucose-6-phosphate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 239 239 Glucose-6-phosphate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 263 263 ATP. {ECO:0000250|UniProtKB:P19367}. FT BINDING 263 263 Glucose-6-phosphate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 266 266 Substrate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 297 297 Substrate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 331 331 Substrate. FT {ECO:0000250|UniProtKB:P19367}. FT BINDING 483 483 Glucose-6-phosphate. FT {ECO:0000250|UniProtKB:P19367}. FT CONFLICT 68 68 T -> S (in Ref. 1; AAR13363). FT {ECO:0000305}. FT CONFLICT 172 172 G -> S (in Ref. 1; AAR13363). FT {ECO:0000305}. FT CONFLICT 504 509 Missing (in Ref. 1; AAR13363). FT {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 //