HXK_EMENI
ID HXK_EMENI Reviewed; 490 AA.
AC P80581; C8VBD5; Q5AW71;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Hexokinase;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:P33284};
GN Name=hxkA; ORFNames=AN7459;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP PROTEIN SEQUENCE OF 210-331.
RC STRAIN=biA1;
RX PubMed=8674991; DOI=10.1111/j.1574-6968.1996.tb08206.x;
RA Ruijter G.J.G., Panneman H., van den Broeck H.C., Bennett J.M., Visser J.;
RT "Characterisation of the Aspergillus nidulans frA1 mutant: hexose
RT phosphorylation and apparent lack of involvement of hexokinase in glucose
RT repression.";
RL FEMS Microbiol. Lett. 139:223-228(1996).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC fructose 6-phosphate, respectively). Mediates the initial step of
CC glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-
CC phosphate. {ECO:0000250|UniProtKB:P33284}.
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:0000250|UniProtKB:P33284};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000250|UniProtKB:P33284};
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:0000250|UniProtKB:P33284};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:P33284};
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:0000250|UniProtKB:P33284};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:P33284}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:P33284}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P33284}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; AACD01000129; EAA62039.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF79423.1; -; Genomic_DNA.
DR RefSeq; XP_680728.1; XM_675636.1.
DR AlphaFoldDB; P80581; -.
DR SMR; P80581; -.
DR STRING; 162425.CADANIAP00000552; -.
DR PRIDE; P80581; -.
DR EnsemblFungi; CBF79423; CBF79423; ANIA_07459.
DR EnsemblFungi; EAA62039; EAA62039; AN7459.2.
DR GeneID; 2869351; -.
DR KEGG; ani:AN7459.2; -.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_5_2_1; -.
DR InParanoid; P80581; -.
DR OMA; IAINCEW; -.
DR OrthoDB; 1153545at2759; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0019158; F:mannokinase activity; IBA:GO_Central.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
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 Allosteric enzyme; ATP-binding; Direct protein sequencing; Glycolysis;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..490
FT /note="Hexokinase"
FT /id="PRO_0000197607"
FT DOMAIN 21..466
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 75..209
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 210..455
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
SQ SEQUENCE 490 AA; 53925 MW; 2CA2F7F97B680812 CRC64;
MVGVGPKRPP SRKGSMSDVP QNLLEHIKHF EEIFTVDTAT LKKIVDHFVN ELTKGLSVEG
GNIPMNVTWV LGFPDGKETG TFLALDMGGT NLRVCEITLT EEKGGFDIIQ SKYRMPEELK
TGEAEELWQY IVDCVEQFIQ FHHENENLSK LPLGFTFSYP ATQDYIDHGV LQRWTKGFDI
DGVEGKDVVP PLEKVFKERG LPIKVAALIN DTTGTLIASS YTDPAMKIGC IFGTGVNAAY
MENAGSIPKL AHMNLPPDMP VAINCEYGAF DNEHIVLPLT KYDHIIDRDS PRPGQQAFEK
MTAGLYLGEI FRLALVDILD TQPGLIFKDQ DTSQLRIPYL LDSSFPAAIE EDPYENLIET
AELVQNMLKI KATRSELELM RRLAELIGTR AARLSACGVA AICKKKNIES CHVGADGSVF
TKYPHFKARG AQALREILDW APSEKDKVTI HAAEDGSGVG AALIAALTLK RVKAGNTAGI
RDAQAMLAMC