ID A0A401KF86_ASPAW Unreviewed; 490 AA.
AC A0A401KF86;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=AAWM_00796 {ECO:0000313|EMBL:GCB17911.1};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB17911.1, ECO:0000313|Proteomes:UP000286921};
RN [1] {ECO:0000313|EMBL:GCB17911.1, ECO:0000313|Proteomes:UP000286921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB17911.1,
RC ECO:0000313|Proteomes:UP000286921};
RA Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT "Aspergillus awamori IFM 58123T.";
RL Submitted (SEP-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB17911.1}.
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DR EMBL; BDHI01000001; GCB17911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401KF86; -.
DR SMR; A0A401KF86; -.
DR STRING; 105351.A0A401KF86; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000286921; 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:UP000286921};
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; 54090 MW; 9DA489EA7768651B CRC64;
MVGIGPKRPP SRKGSMADVP QNLLQQIKDF EDQFTVDRSK LKQIVNHFVK ELEKGLSVEG
GNIPMNVTWV LGFPDGDEQG TFLALDMGGT NLRVCEITLT QEKGAFDITQ SKYRMPEELK
TGTAEELWEY IADCLQQFIE SHHENEKISK LPLGFTFSYP ATQDYIDHGV LQRWTKGFDI
DGVEGHDVVP PLEAILQKRG LPIKVAALIN DTTGTLIASS YTDSDMKIGC IFGTGVNAAY
MENAGSIPKL AHMNLPADMP VAINCEYGAF DNEHIVLPLT KYDHIIDRDS PRPGQQAFEK
MTAGLYLGEI FRLALMDLVE NRPGLIFNGQ DTTKLRKPYI LDASFLAAIE EDPYENLEET
EELMERELNI KATPAELEMI RRLAELIGTR AARLSACGVA AICTKKKIDS CHVGADGSVF
TKYPHFKARG AKALREILDW APEEQDKVTI MAAEDGSGVG AALIAALTLK RVKAGNLAGI
RNMADMKTLL
//
