ID A0A2I2GDW3_9EURO Unreviewed; 622 AA.
AC A0A2I2GDW3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=P170DRAFT_446229 {ECO:0000313|EMBL:PLB51084.1};
OS Aspergillus steynii IBT 23096.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB51084.1, ECO:0000313|Proteomes:UP000234275};
RN [1] {ECO:0000313|EMBL:PLB51084.1, ECO:0000313|Proteomes:UP000234275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB51084.1,
RC ECO:0000313|Proteomes:UP000234275};
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 (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PLB51084.1}.
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DR EMBL; MSFO01000003; PLB51084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I2GDW3; -.
DR STRING; 1392250.A0A2I2GDW3; -.
DR VEuPathDB; FungiDB:P170DRAFT_446229; -.
DR OrthoDB; 5481886at2759; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000234275; Unassembled WGS sequence.
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 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; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF29; PHOSPHOTRANSFERASE; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 50..288
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 300..614
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 68196 MW; 36F96D658E019132 CRC64;
MAPVNPISAE ETKDEDHDHL HEDPIDVEED EEEDDLDPLQ KEHLERHRVL DQFLSPLALD
EAVLYKLARR FSGVYRKLAL ESEEQFLPTP VTNLPTGLET GRYLAIDVGG SNLRVAFIEL
LGESADSDIR SGDASNKSRD TIRKAQRQRV KRTLEKAWPI QEHLKMDKAE DLFAWIGDCI
AEVVAESLTS DATKGTIPEE LEMGITFSFP IMQESLAEAT LMPMGKGFAI TSDLNLRKIL
LNGYEKHTKR PGDEEEPSAK RRKLYSLPKL KISAITNDAV ATLTSLAYEV KSLPNSRVAM
GIIVGTGCNA TIPMKLESLH DSKARHVKLR NSAAQETVVN TEWTLSGALP PLKELDIITK
WDVELDRACA RPGFQPFEYM TGGRYIGELV RLIIIDYLTT VYGVPEKALP ANIIQDYALT
TSYISDKVAR ARTDQELADE LGSSLSPPEG SDWRWDAITA GAFRKIARTV QRRSAGLIAA
AVVGLLACAR EIELKVDSNE NSPLNSSATS PVHNGGSHEF TPPTLGVPGT THSRGPIVPV
LSPTPTPADW QSGPEELVVA YTGGIIQHYP NFKEMCQQFI DRLIMRTGPQ KSGKSAFLRE
ASDGGVIGAG VLAGMVGNNP SL
//
