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Database: UniProt
Entry: A0A0R3W4T6_TAEAS
LinkDB: A0A0R3W4T6_TAEAS
Original site: A0A0R3W4T6_TAEAS 
ID   A0A0R3W4T6_TAEAS        Unreviewed;       337 AA.
AC   A0A0R3W4T6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyridoxal kinase {ECO:0000256|ARBA:ARBA00018134};
DE            EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE   AltName: Full=Pyridoxine kinase {ECO:0000256|ARBA:ARBA00032808};
GN   ORFNames=TASK_LOCUS5081 {ECO:0000313|EMBL:VDK34472.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000508001-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000508001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK34472.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC         Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC         EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00000330};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC         Evidence={ECO:0000256|ARBA:ARBA00000330};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxamine = ADP + H(+) + pyridoxamine 5'-phosphate;
CC         Xref=Rhea:RHEA:25104, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57761, ChEBI:CHEBI:58451, ChEBI:CHEBI:456216;
CC         EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00001079};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001079};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + pyridoxine = ADP + H(+) + pyridoxine 5'-phosphate;
CC         Xref=Rhea:RHEA:25108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58589, ChEBI:CHEBI:456216;
CC         EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00000046};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109;
CC         Evidence={ECO:0000256|ARBA:ARBA00000046};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxal: step 1/1. {ECO:0000256|ARBA:ARBA00005210}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxamine 5'-phosphate from pyridoxamine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004750}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxine 5'-phosphate from pyridoxine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004835}.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
CC       {ECO:0000256|ARBA:ARBA00008805}.
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DR   EMBL; UYRS01018390; VDK34472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3W4T6; -.
DR   STRING; 60517.A0A0R3W4T6; -.
DR   WBParaSite; TASK_0000508001-mRNA-1; TASK_0000508001-mRNA-1; TASK_0000508001.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; Unassembled WGS sequence.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR   CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   NCBIfam; TIGR00687; pyridox_kin; 1.
DR   PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR   PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; Ribokinase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT   DOMAIN          81..185
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   337 AA;  38029 MW;  7B6B1B1E4DA76D37 CRC64;
     MESKRVLSVQ SHVVHGYVGN KSAVFPLQLH NYEVDNINSV QLSCHTQYIH CSGQVLTRKH
     LDSIYDSLRQ NGSANYDALL TGYVGDSDFL IQLAEIAVET KSDNPYCRFY CDPVIGDNGH
     IYVPEELIPI YREKILPVAD ILLPNQFEAE LLTGCKITDE DSAFHCIDLL HSTHGIPTII
     LSSTELFFED EQGLKQLATY ISYRPDLAEL RKCGKFSGDL GQKGKTFSMN GSFFSQRVRA
     LFPKLEATFF GTGDLFSSLT LIYFEKNNGN LDMAKVLYKI QCTMHAVLKR TLEYAENLNS
     DPTNMLQKSD RYELRLIQSA KDILNPPEFA SVQVTLL
//
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