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PDXY_DEIRA
ID   PDXY_DEIRA              Reviewed;         298 AA.
AC   Q9RYX0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Pyridoxal kinase PdxY {ECO:0000255|HAMAP-Rule:MF_01639};
DE            Short=PL kinase {ECO:0000255|HAMAP-Rule:MF_01639};
DE            EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01639};
GN   Name=pdxY {ECO:0000255|HAMAP-Rule:MF_01639}; OrderedLocusNames=DR_A0184;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal
CC       5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
CC       {ECO:0000255|HAMAP-Rule:MF_01639}.
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:0000255|HAMAP-Rule:MF_01639};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01639};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC       5'-phosphate from pyridoxal: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01639}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01639}.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01639}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF12189.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE001825; AAF12189.1; ALT_INIT; Genomic_DNA.
DR   PIR; B75615; B75615.
DR   RefSeq; NP_285508.1; NC_001264.1.
DR   AlphaFoldDB; Q9RYX0; -.
DR   SMR; Q9RYX0; -.
DR   STRING; 243230.DR_A0184; -.
DR   EnsemblBacteria; AAF12189; AAF12189; DR_A0184.
DR   KEGG; dra:DR_A0184; -.
DR   PATRIC; fig|243230.17.peg.3073; -.
DR   eggNOG; COG2240; Bacteria.
DR   HOGENOM; CLU_046496_3_1_0; -.
DR   InParanoid; Q9RYX0; -.
DR   OMA; CPNQLEL; -.
DR   OrthoDB; 1480223at2; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000002524; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR   CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   HAMAP; MF_01639; PdxY; 1.
DR   InterPro; IPR013749; PM/HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlKinase.
DR   InterPro; IPR023685; Pyridoxal_kinase_PdxY.
DR   InterPro; IPR029056; Ribokinase-like.
DR   PANTHER; PTHR10534; PTHR10534; 1.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..298
FT                   /note="Pyridoxal kinase PdxY"
FT                   /id="PRO_0000269805"
FT   BINDING         17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ   SEQUENCE   298 AA;  31540 MW;  8C72ED98C98A4649 CRC64;
     MDSVTPTLPR NILSIQSWVS YGHVGNAAAI FPLQRLGFEV WGVHTVQFSN HTGYGAWTGP
     VFEPGVIAEL LDGIEARGVL PQCDGVLSGY VGSGGTVAAV VGAVGRVRQA HPQALYCCDP
     VMGDVGRGVF VHPDLPALIA AQAIPAADIV TPNQFELELL TGQKVETLAD ALAAAHALRE
     RLNPAGPRIV LLTSLVRADA PASSIETLAV TGEGSWLCRT PLLPLDPPRN GTGDAIAALF
     YGQFLRTGSA EQALTLSMSA LYALLDLTHR LGTREIQLVA AQGEFERPRH LFAAERVE
 
 
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