ID W6ZKH2_COCMI Unreviewed; 526 AA.
AC W6ZKH2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN ORFNames=COCMIDRAFT_21899 {ECO:0000313|EMBL:EUC50585.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC50585.1};
RN [1] {ECO:0000313|EMBL:EUC50585.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC50585.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; KI963922; EUC50585.1; -; Genomic_DNA.
DR RefSeq; XP_007682822.1; XM_007684632.1.
DR AlphaFoldDB; W6ZKH2; -.
DR GeneID; 19120134; -.
DR KEGG; bor:COCMIDRAFT_21899; -.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_4_0_1; -.
DR OrthoDB; 5481886at2759; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000054032; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 17..238
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 250..521
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 526 AA; 56492 MW; 790B2D38D1D6C4B8 CRC64;
MASTDAAVPI DAFTSLINTT TLLDLARRFS ATYSHLARTS TEHFLATPVT ALPTGKEKGK
FLSIDVGGTN LRVGFVELIG EPDASAGSER SRSSTIGDNV FAQINRSHDK NWPIGDHLKM
DQAEDLFAWI GDCIAEVVKG ALDEQESSDS QVSSPLGDEI LLGITFSFPM AQTRLSEATL
LPMGKGFAIT SDLNLGKMLL AGYARHCDAS QQNKPPLPRI RVAAITNDTV ATFASLAYAV
KASPNSRVSM GLIVGTGTNA TVPMKLDHLH PAKKSALANP DAVETVVINT EWTIRGTDKP
LIDLNIKTPW DMTLDANSDA PGFQPFEYMT SGRYLGEIVR LIFIDVVSKD SSVQIPPSLQ
TKNALPTRFL SEVIARKGGR IVQQELENRY PDASPSDDPF WTVDRVEMIR DIAEAVQQRS
SALVAAACVG LLNCVGEVSL DGAKAPSNGT QHSSKGKREI EELVIAYAGG TISQYPKWLQ
TCQQWIDILV EEGSAANSSK QVTLKEAKDG GIIGAGVLAA MTDDMA
//