ID A0A0L8H0T9_OCTBM Unreviewed; 302 AA.
AC A0A0L8H0T9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, 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=OCBIM_22024653mg {ECO:0000313|EMBL:KOF82906.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF82906.1};
RN [1] {ECO:0000313|EMBL:KOF82906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF82906.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF82906.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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}.
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; KQ419607; KOF82906.1; -; Genomic_DNA.
DR RefSeq; XP_014776361.1; XM_014920875.1.
DR AlphaFoldDB; A0A0L8H0T9; -.
DR STRING; 37653.A0A0L8H0T9; -.
DR EnsemblMetazoa; Ocbimv22024653m; Ocbimv22024653m.p; Ocbimv22024653m.g.
DR EnsemblMetazoa; XM_014920875.1; XP_014776361.1; LOC106873490.
DR GeneID; 106873490; -.
DR KEGG; obi:106873490; -.
DR OMA; CPNQLEL; -.
DR OrthoDB; 5472295at2759; -.
DR UniPathway; UPA01068; UER00298.
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;
FT DOMAIN 83..265
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 302 AA; 33562 MW; 0F2F48B65D25E053 CRC64;
MLDDLEMPRV LTIQSTVVSG YVGNKVALFP LQLHGFETSA INSVQLSNHT GYQYFKGQVL
GAKEIDELYE GLKLNKLNSF SFILTGYMAS KSFLEKVGEA IREMKQENPN TIYLCDPVMG
DNGEMYVPEE LLPVYRDILV PLSDITVPNQ FEAECLTGIK INNLTDSIKA IECIHKLGVQ
TVIMSSSTLG KGTNTLVCIA SRYTESGVER YKIEFPHIDA IFVGTGDLFS ATILIWLHKD
KNLKTALEKT VSVIQFVIQK TIAAASKTAQ GRSDSAANME LKLIQCKKEL EDPKIQYFAE
TL
//
