ID A0A319DSZ6_ASPSB Unreviewed; 490 AA.
AC A0A319DSZ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=BO78DRAFT_401806 {ECO:0000313|EMBL:PYI00827.1};
OS Aspergillus sclerotiicarbonarius (strain CBS 121057 / IBT 28362).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448318 {ECO:0000313|EMBL:PYI00827.1, ECO:0000313|Proteomes:UP000248423};
RN [1] {ECO:0000313|EMBL:PYI00827.1, ECO:0000313|Proteomes:UP000248423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121057 {ECO:0000313|EMBL:PYI00827.1,
RC ECO:0000313|Proteomes:UP000248423};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004888}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; KZ826434; PYI00827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319DSZ6; -.
DR STRING; 1448318.A0A319DSZ6; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000248423; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 1.10.287.1250; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
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; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362007};
KW Reference proteome {ECO:0000313|Proteomes:UP000248423};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 27..221
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 227..467
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 490 AA; 54092 MW; 19C6DE4385675344 CRC64;
MVGLGPKRPH SRKGSMADVP QNLLQQIKDF EEHFTVDRTK LKGIVDHFIK ELEKGLSVEG
GNIPMNVTWV LGFPDGDEQG TFLALDMGGT NLRVCEITLT QEKGAFDITQ SKYRMPEELK
TGTAEELWEY IADCLQQFIE SHHENEKVSK LPLGFTFSYP ATQDYIDHGV LQRWTKGFDI
DGVEGEDVVP PLESILQKRG LPIKVAALIN DTTGTLIASS YTDSAMKIGC IFGTGVNAAY
MENVGSVPKL AHMNLPPDMP VAINCEYGAF DNEHIVLPLT KYDHIIDRDS PRPGQQAFEK
MTAGLYLGEI FRLALVDLVE NRPGLIFNGQ DTTKLRKPYI LDASFLAAIE EDPYENLEET
EELLERELNI KATQPELEMI RRLAELIGTR AARLSACGVA AICKKKGLES CHVGADGSVF
TKYPHFKARG AQALREILDW APEEKDKVTI MAAEDGSGVG AALIAALTLK RVKAGNLAGI
RNMAEMQTLL
//