ID J5PKW1_SACK1 Unreviewed; 500 AA.
AC J5PKW1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN Name=YCL040W {ECO:0000313|EMBL:EJT42888.1};
GN Synonyms=SKDI03G0310 {ECO:0000313|EMBL:CAI4056425.1};
GN ORFNames=SKDI_03G0310 {ECO:0000313|EMBL:CAI4056425.1}, SKUD_207205
GN {ECO:0000313|EMBL:EJT42888.1};
OS Saccharomyces kudriavzevii (strain ATCC MYA-4449 / AS 2.2408 / CBS 8840 /
OS NBRC 1802 / NCYC 2889) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=226230 {ECO:0000313|EMBL:EJT42888.1, ECO:0000313|Proteomes:UP000002753};
RN [1] {ECO:0000313|EMBL:EJT42888.1, ECO:0000313|Proteomes:UP000002753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753}, and IFO 1802
RC {ECO:0000313|EMBL:EJT42888.1};
RX PubMed=12775844; DOI=10.1126/science.1084337;
RA Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J.,
RA Waterston R., Cohen B.A., Johnston M.;
RT "Finding functional features in Saccharomyces genomes by phylogenetic
RT footprinting.";
RL Science 301:71-76(2003).
RN [2] {ECO:0000313|EMBL:EJT42888.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT42888.1};
RA Cliften P.F., Johnston M.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000002753}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4449 / AS 2.2408 / CBS 8840 / NBRC 1802 / NCYC 2889
RC {ECO:0000313|Proteomes:UP000002753};
RX PubMed=22384314; DOI=10.1534/g3.111.000273;
RA Scannell D.R., Zill O.A., Rokas A., Payen C., Dunham M.J., Eisen M.B.,
RA Rine J., Johnston M., Hittinger C.T.;
RT "The awesome power of yeast evolutionary genetics: New genome sequences and
RT strain resources for the Saccharomyces sensu stricto genus.";
RL G3 (Bethesda) 1:11-25(2011).
RN [4] {ECO:0000313|EMBL:EJT42888.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO 1802 {ECO:0000313|EMBL:EJT42888.1};
RA Cliften P., Hittinger C.T., Wang B., Sudarsanam P., Desikan A., Fulton L.,
RA Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:CAI4056425.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFO1802 {ECO:0000313|EMBL:CAI4056425.1};
RA Byrne P K.;
RL Submitted (OCT-2022) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; OX365898; CAI4056425.1; -; Genomic_DNA.
DR EMBL; AACI03001033; EJT42888.1; -; Genomic_DNA.
DR AlphaFoldDB; J5PKW1; -.
DR STRING; 226230.J5PKW1; -.
DR HOGENOM; CLU_014393_5_0_1; -.
DR UniPathway; UPA00109; UER00180.
DR Proteomes; UP000002753; Unassembled WGS sequence.
DR Proteomes; UP001162087; Chromosome 3.
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; 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:SF30; GLUCOKINASE-1-RELATED; 1.
DR PANTHER; PTHR19443; HEXOKINASE; 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:UP000002753};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 18..228
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 246..499
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 500 AA; 55495 MW; 729920EDD764A9D1 CRC64;
MSFDDLHKAT ERAVIQAVDQ ICDEFEVTPE KLDELTAYFI EQMEKGLTPP QEGHTLASDK
GLPMIPAFVT GSPNGTERGV LLAADLGGTN FRICSVNLHG DHSFSMEQMK SKIPDDLLDD
ENVTSDDLFG FLARRTLAFM KKYHPDELAQ GKDAKPMKLG FTFSYPVDQT SLNSGTLIRW
TKGFRIADTV GKDVVQLYQE QLRAQGMPMV KVVALTNDTV GTYLSHCYTS DNTDSMTSGE
ISEPVIGCIF GTGTNGCYME EINKITKLPQ ELRDKLIKEG KTHMIINVEW GSFDNELKHL
PTTKYDVVID QKLSTNPGFH LFEKRVSGMF LGEVLRNVLV DLHSQGLLLQ QYRTKEQLPR
HLTTPFQLSS EVLSHIEIDD STGLRETELS LLQSLRLPTT PTERMQIQKL VRAISRRSAY
LAAVPLAAIL IKTNALNKRY HGEVEIGCDG SVVEYYPGFR SMLRHALALS PLGAEGERKV
HLKIAKDGSG VGAALCALVA
//
