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Database: UniProt
Entry: A0A0C2CBI2_9BILA
LinkDB: A0A0C2CBI2_9BILA
Original site: A0A0C2CBI2_9BILA 
ID   A0A0C2CBI2_9BILA        Unreviewed;       206 AA.
AC   A0A0C2CBI2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE            EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN   ORFNames=ANCDUO_16184 {ECO:0000313|EMBL:KIH53683.1};
OS   Ancylostoma duodenale.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH53683.1, ECO:0000313|Proteomes:UP000054047};
RN   [1] {ECO:0000313|EMBL:KIH53683.1, ECO:0000313|Proteomes:UP000054047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zhejiang {ECO:0000313|EMBL:KIH53683.1,
RC   ECO:0000313|Proteomes:UP000054047};
RA   Mitreva M.;
RT   "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL   Submitted (DEC-2013) 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|RuleBase:RU362007}.
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DR   EMBL; KN740637; KIH53683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2CBI2; -.
DR   Proteomes; UP000054047; 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-KW.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
DR   Gene3D; 3.40.367.20; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   PANTHER; PTHR19443; HEXOKINASE; 1.
DR   PANTHER; PTHR19443:SF77; PHOSPHOTRANSFERASE; 1.
DR   Pfam; PF03727; Hexokinase_2; 1.
DR   PRINTS; PR00475; HEXOKINASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   PROSITE; PS51748; HEXOKINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362007};
KW   Glycolysis {ECO:0000256|RuleBase:RU362007};
KW   Kinase {ECO:0000256|RuleBase:RU362007, ECO:0000313|EMBL:KIH53683.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362007};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|RuleBase:RU362007}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..206
FT                   /note="Phosphotransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002159047"
FT   DOMAIN          15..194
FT                   /note="Hexokinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03727"
SQ   SEQUENCE   206 AA;  23602 MW;  45F800F6352157C1 CRC64;
     MFICGITFFI WFIFQMIIDT EWGGFGDRGE AEYIFTQYDK IIDERSDHPG VNSLDKLVAG
     MCMGEVVRLV LDKLCTHKVL FNGNGSKILS TTGSFPTKYI SEILHDDCGS YSNTRQIMDE
     LAIDDYTFSD MLLFREVCLV VSRRSANLSA AAIACVLNRV RRPRMLVAID GSTYKYHPFF
     DHWVTDKVKE LIDPGLEVNH YFLFSF
//
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