ID A0A0V0V451_9BILA Unreviewed; 746 AA.
AC A0A0V0V451;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=hexokinase {ECO:0000256|ARBA:ARBA00012324};
DE EC=2.7.1.1 {ECO:0000256|ARBA:ARBA00012324};
DE Flags: Fragment;
GN ORFNames=T09_4177 {ECO:0000313|EMBL:KRX58265.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX58265.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX58265.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX58265.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC residues to glutamate, an important step in N-end rule pathway of
CC protein degradation. Conversion of the resulting N-terminal glutamine
CC to glutamate renders the protein susceptible to arginylation,
CC polyubiquitination and degradation as specified by the N-end rule. Does
CC not act on substrates with internal or C-terminal glutamine and does
CC not act on non-glutamine residues in any position.
CC {ECO:0000256|ARBA:ARBA00003923}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000256|ARBA:ARBA00000435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000417};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000256|ARBA:ARBA00000417};
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}.
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:KRX58265.1}.
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DR EMBL; JYDN01000088; KRX58265.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V451; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019318; P:hexose metabolic 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 Gene3D; 3.10.620.10; Protein N-terminal glutamine amidohydrolase, alpha beta roll; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR PANTHER; PTHR19443; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF77; PHOSPHOTRANSFERASE; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 2.
DR Pfam; PF09764; Nt_Gln_amidase; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRX58265.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 159..352
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 360..501
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 504..570
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
FT DOMAIN 577..745
FT /note="Protein N-terminal glutamine amidohydrolase alpha
FT beta roll"
FT /evidence="ECO:0000259|Pfam:PF09764"
FT NON_TER 746
FT /evidence="ECO:0000313|EMBL:KRX58265.1"
SQ SEQUENCE 746 AA; 84589 MW; EB096FEBE4374DF0 CRC64;
MEQRRKFHRP VLVRVVLVSV TLEILMVFSS SPAAFFTLVR SRGADAYLIT RGHLDADIRP
VQCDIRYGWI RRGKRRAESQ RAEQQKTANT TKLVAFHQLV RLLCCHSSSS PNKLVRPFKL
RIVNFRRFCF LELLNLKKML SIVQFITDAF KRKKQKFTLE SVLAEFILDN DALRRMMYIM
DRQMTSGLAG GLKESTIAML PSFVPVLPDG TECGKYMAID LGGTNLRVML MNIAANADDT
TAESCNFRMP QNAMTGTGEE LFDFIASCME SVLRNKKLLD EPIKMGFTFS YPCDQTSLCS
AKLLRWTKGF NASGVEGEDV VKLLQTAIHK RNLKITVMAL MNDTVGTQVA TAHDMRQCEL
GVIVATGTNA SYMEDVKKIP KLKDVDFPYE KMIIDTEWGG FGDGGEAEFI KTQYDRIVDE
RSVHPGVQCF DKMVAGMYMG ELVRLVIEKL VKGNLIFRGV GSQLLFTPNT FPTKFISEIL
ADEGGNMVQT RQILDELGIE TYVYTIACVL NRIGKKKAIV GIDGSTYRFH PFLHSWVKDK
VRELLDPNID FHLVQAGDGS GRGAALVAAI ADKLNLEENV WHLSKQLISA FPTSNCRVCF
LTNCKRKVSL WHQRTGDPNF EGFVVWDYHV FAMLHHDQQG ELIFDLDTTL QFPCSAKEYV
EKAIRPDCEC HNNRRLFRVV DAKLYIEKFA SDRSHMISPE TFAHPPPWPI IVTHNCQNNL
SKWLEVAVDR CPHTDSYGCV FDLEQV
//