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Database: UniProt
Entry: V4AMQ3_LOTGI
LinkDB: V4AMQ3_LOTGI
Original site: V4AMQ3_LOTGI 
ID   V4AMQ3_LOTGI            Unreviewed;       306 AA.
AC   V4AMQ3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=LOTGIDRAFT_144857 {ECO:0000313|EMBL:ESO94876.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO94876.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO94876.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
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; KB201747; ESO94876.1; -; Genomic_DNA.
DR   RefSeq; XP_009054441.1; XM_009056193.1.
DR   AlphaFoldDB; V4AMQ3; -.
DR   STRING; 225164.V4AMQ3; -.
DR   EnsemblMetazoa; LotgiT144857; LotgiP144857; LotgiG144857.
DR   GeneID; 20234886; -.
DR   KEGG; lgi:LOTGIDRAFT_144857; -.
DR   CTD; 20234886; -.
DR   HOGENOM; CLU_046496_1_1_1; -.
DR   OMA; CPNQLEL; -.
DR   OrthoDB; 5472295at2759; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000030746; 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:UP000030746}.
FT   DOMAIN          77..270
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   306 AA;  34061 MW;  61BAA9A4D01BB28A CRC64;
     MSETELRVLS IQSSVVYGYV GNKCATFPLQ VLGFDVSTIN SVQFSNHKGY GYCKGQVLNH
     SEVSELYDGL KHNNLINFSH VLTGYIGSKC FLEKVSEMIK EIKENNPKLI YVCDPVMGDN
     GKMYVPQDLL PVYRDMIIPL ADILTPNQFE LEVLTEKKIE GLEDALSAID ILHNRGVPTV
     VLSSSNLGTS GTLLCVASSV KSKFYYFCDG KKEIYKIEFP LLPAFFSGTG DLFAASLLAW
     SQKDQNLKLA LEKTVSTVQA VIKRTLNYAK SLSAENEPSK KQLELRIIQS KKDLENPEII
     HHAVPV
//
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