ID F9FI99_FUSOF Unreviewed; 540 AA.
AC F9FI99;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=FOXB_06128 {ECO:0000313|EMBL:EGU83348.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU83348.1};
RN [1] {ECO:0000313|EMBL:EGU83348.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83348.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU83348.1}.
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DR EMBL; AFQF01001866; EGU83348.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FI99; -.
DR STRING; 660025.F9FI99; -.
DR UniPathway; UPA00109; UER00180.
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; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443:SF30; GLUCOKINASE-1-RELATED; 1.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 2.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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|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 14..210
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 221..410
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 479..537
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 540 AA; 58789 MW; 37B292FFDCFD09C9 CRC64;
MLEDGLGDSQ QATVQSVAQE FEVGNEKIQE ITNYFVKQIK HGLKDKHAYQ IPSFVTQIPS
GREKGLFLAV DLGGTNCRVC AVTLHGDSTF DVFQRKHLVP HDIRVHSSHK PLFHFIALKI
QDLLREHKSS GSSDSSEACF NLGFTFSFTC EQTSISSGTL VHWDKGWDIP STLGQDPCAL
LQEAIDEISL PVRIRVLAND AVGTLLTRAY TSKTKNSTLA SIILGTGTNA AYIERMSNIQ
RLDTTADRAH HSNSDGFMVI NTEWGSWDDG LKVLPQTRFD KLVDESSSDP GCGLLEKMVS
GMYLGELLRL SLLDLMRHGA LDMSFPDGSP VYIHMGIESA FLSKIAESKP ENSLSALSCI
TDTLVATGVT SRDLRTIQML ATVIVKRSAR LVGAGLAAIL IQSGRLDTSG MSQKTGLGAH
THQIQDKSTS TQIGSRRNTL TRFIRRMFGC IRPEEPSPIS TNGSSYDSKD TLESSELADE
VIDIAVDGSL FEFHTAFESF MRTALRDVEA IGKANEARIK IELTRDGSGT GAALIAAAAA
//
