ID U6N4G6_9EIME Unreviewed; 584 AA.
AC U6N4G6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
DE Flags: Fragment;
GN ORFNames=ENH_00079810 {ECO:0000313|EMBL:CDJ70184.1};
OS Eimeria necatrix.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51315 {ECO:0000313|EMBL:CDJ70184.1};
RN [1] {ECO:0000313|EMBL:CDJ70184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ70184.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ70184.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ70184.1};
RA Aslett M.;
RL Submitted (OCT-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG725887; CDJ70184.1; -; Genomic_DNA.
DR RefSeq; XP_013438650.1; XM_013583196.1.
DR AlphaFoldDB; U6N4G6; -.
DR GeneID; 25478110; -.
DR VEuPathDB; ToxoDB:ENH_00079810; -.
DR OrthoDB; 5481886at2759; -.
DR UniPathway; UPA00109; UER00180.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008865; F:fructokinase activity; IEA:RHEA.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 310..527
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 538..583
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 584
FT /evidence="ECO:0000313|EMBL:CDJ70184.1"
SQ SEQUENCE 584 AA; 62417 MW; D39BFEE5233950C2 CRC64;
MSEAPPTPPS ERGPHRAFFL RRRPRRNEGA PSSNKQQQVA AATEAAAAAA AAAAASRALA
TLQSLPTESC GSTSSSSNRS SSNSSSSSSK SNLQLANILE RETTAGSADG AGSFSAAAAA
AAAAITPAAA AAAITPAAAA AAITPAAAAP KRAARSRLPE VWAAAKWLLF STRVVGWLVV
LLQLLLLLLL LQQREELLLQ REALQGQTVR EQLEQQQQLL QQRSCHCKPC AAAAAAAAAA
AAEEWIDIKD RFKHSQKEVE LSVAALLRKE EPLSSRAAAP SETVQQQQQQ QQQQQLEQRK
TRRRLPVLLL QQVLAPLRLS KEKLQELSKT FSDELLRGLE MHKRHGLQWV PEECSLRMLD
SCVSAIPSGH EKGVFYALDF GGTNVRAVRC ELLGGGRIQA QQFLKNLYEC GGEIDLMARE
TSASQLFDVL ANCVGELVEE NNEKEILKNK KAKLGFTFSF PCAQQSLNNS VLESWTKGFA
TGHDTDDPVV GKDVVPLLAA AFERQGLGLE CEAVVNDTVG TLLSCAYQKS PGSPPCTVGV
ILGTGANCCY WEPQAAAFGY KGSIVNVECG NFNKNLPTTP ADQA
//