ID   B8NPD5_ASPFN            Unreviewed;       490 AA.
AC   B8NPD5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=AFLA_130070 {ECO:0000313|EMBL:EED48784.1}, G4B84_002766
GN   {ECO:0000313|EMBL:QMW27477.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED48784.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED48784.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC   {ECO:0000313|EMBL:EED48784.1};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2] {ECO:0000313|EMBL:QMW27477.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW27477.1,
RC   ECO:0000313|Proteomes:UP000515286};
RA   Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA   Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA   Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA   Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT   "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT   Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT   Aflatoxin Production.";
RL   Submitted (JUL-2020) 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; EQ963481; EED48784.1; -; Genomic_DNA.
DR   EMBL; CP059867; QMW27477.1; -; Genomic_DNA.
DR   RefSeq; XP_002382200.1; XM_002382159.1.
DR   AlphaFoldDB; B8NPD5; -.
DR   STRING; 332952.B8NPD5; -.
DR   EnsemblFungi; EED48784; EED48784; AFLA_130070.
DR   VEuPathDB; FungiDB:AFLA_012843; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_2_1; -.
DR   OMA; ADCVQQF; -.
DR   OrthoDB; 5481886at2759; -.
DR   UniPathway; UPA00109; UER00180.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-UniRule.
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   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;  54147 MW;  28B891A5E6E37FF1 CRC64;
     MVGIGPKRPP SRKGSMHELP QNLLEQIKQF EDIFTVDGAK LKQIADHFVK ELEKGLSVEG
     GNIPMNVTWV MGFPDGDEQG TFLALDMGGT NLRVCEITLT EEKGAFDITQ SKYRMPEELK
     TGTAEELWEY IADCLQQFIE SHHENEKLSK LPLGFTFSYP ATQEYIDHGV LQRWTKGFDI
     DGVEGQDVVP PLEAILKKRG LPIKVAALIN DTTGTLIASS YTDSDMKIGC IFGTGVNAAY
     MEHCGSVPKL AHKNLPPDMP VAINCEYGAF DNEHVVLPLT KYDIIIDRDS PRPGQQAFEK
     MTAGLYLGEI FRLALLDLLE TRPGLIFQGQ DTSQLRKPYL LDASFLAAIE DDPYENLQET
     QELMERKLNI KATQQELEMI RRLAELIGTR AARLSACGVA AICKKKNIES CHVGADGSVF
     TKYPHFKARG AQALREILDW APNEKDKVVI MAAEDGSGVG AALIAALTLK RVKAGISCGI
     RDMADMQSLI
//