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Database: UniProt
Entry: A0A8I6RCS6_CIMLE
LinkDB: A0A8I6RCS6_CIMLE
Original site: A0A8I6RCS6_CIMLE 
ID   A0A8I6RCS6_CIMLE        Unreviewed;       331 AA.
AC   A0A8I6RCS6;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   28-JAN-2026, entry version 13.
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};
OS   Cimex lectularius (Bed bug) (Acanthia lectularia).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Cimicidae; Cimex.
OX   NCBI_TaxID=79782 {ECO:0000313|EnsemblMetazoa:XP_014242769.2, ECO:0000313|Proteomes:UP000494040};
RN   [1] {ECO:0000313|EnsemblMetazoa:XP_014242769.2}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-2022) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyridoxal + ATP = pyridoxal 5'-phosphate + ADP + H(+);
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:ARBA00047377};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225;
CC         Evidence={ECO:0000256|ARBA:ARBA00047377};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyridoxamine + ATP = pyridoxamine 5'-phosphate + ADP + H(+);
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:ARBA00047310};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25105;
CC         Evidence={ECO:0000256|ARBA:ARBA00047310};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyridoxine + ATP = pyridoxine 5'-phosphate + ADP + H(+);
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:ARBA00048524};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25109;
CC         Evidence={ECO:0000256|ARBA:ARBA00048524};
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   RefSeq; XP_014242769.2; XM_014387283.2.
DR   AlphaFoldDB; A0A8I6RCS6; -.
DR   EnsemblMetazoa; XM_014387283.2; XP_014242769.2; LOC106662866.
DR   GeneID; 106662866; -.
DR   OrthoDB; 2104723at2759; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000494040; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494040};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          124..296
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   331 AA;  36643 MW;  F332817D917EB827 CRC64;
     MTVTQNQLHK ISYVTLSTDI EAHSIVFQTV ADMESPRVLS IQSHVVHGYV GNKSATFPLQ
     VLGFEVDPIN SVQLSNHTGY KSFKGQILNE NDLNDLIESL KHNNLLNYTH LLTGYVGSPS
     FLNKIVDLVK ELRQINPNLV YVCDPVMGDN GKLYVPESLL PIYQDLLIPL ADVITPNQFE
     LELLTGHKIN SIDDAWTAIN TFHNKSNCST VIVSSSNLGT ENELIALASS NAGGKEKRVL
     LKFPKLPGNF TGTGDLFAAL FLAWNYKTKN NLTKSLEYTI STLQSLLKRT LNIAKESSNG
     QPLTHAQLEL KIIQSKNDIE DPKVTVQAVE L
//
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