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Database: UniProt
Entry: T1JPG7_STRMM
LinkDB: T1JPG7_STRMM
Original site: T1JPG7_STRMM 
ID   T1JPG7_STRMM            Unreviewed;       354 AA.
AC   T1JPG7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, 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};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR015744-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR015744-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
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; JH432004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1JPG7; -.
DR   STRING; 126957.T1JPG7; -.
DR   EnsemblMetazoa; SMAR015744-RA; SMAR015744-PA; SMAR015744.
DR   eggNOG; KOG2599; Eukaryota.
DR   HOGENOM; CLU_046496_1_1_1; -.
DR   OMA; CPNQLEL; -.
DR   OrthoDB; 5472295at2759; -.
DR   PhylomeDB; T1JPG7; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000014500; 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:UP000014500}.
FT   DOMAIN          116..224
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   354 AA;  39399 MW;  CD90CAA60C725731 CRC64;
     MHRCKNISFA NLKLLSAEAR RCKLFCRGII MNTCDFAEGR VLSIQSHVVS GYVGNKSATF
     PLQILGFEVD AINSVQFSNH TGYAYFKGQV LDSTQLEQLM TGLRFNNILN YTHLLTGYIG
     NESFVRKIAD VAKELKEINP GVIYVCDPVM GDNGQMYVPP EILPIYQNEI LPIANIITPN
     QFEAEILTGI TIKTEEDAWE AVEKIHSQGP ETVIITSTNL GPEDKLMGLA SNSKGLSFLL
     HQLKCMSKVE FIHLDGKKLR VRLNIPKLAC SFTGTGDLFT ACFLAWMFKT NGDIKIASEK
     TVSTVQDVLK RTFKAAENKP LESDLAWVAA TELKLIQSKN DIENPKTPFE AQIV
//
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