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PDXY_BURP1
ID   PDXY_BURP1              Reviewed;         287 AA.
AC   Q3JQA6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 75.
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};
GN   OrderedLocusNames=BURPS1710b_2863;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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=ABA49930.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000124; ABA49930.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004538085.1; NC_007434.1.
DR   AlphaFoldDB; Q3JQA6; -.
DR   SMR; Q3JQA6; -.
DR   EnsemblBacteria; ABA49930; ABA49930; BURPS1710b_2863.
DR   KEGG; bpm:BURPS1710b_2863; -.
DR   HOGENOM; CLU_046496_3_0_4; -.
DR   OrthoDB; 1480223at2; -.
DR   UniPathway; UPA01068; UER00298.
DR   Proteomes; UP000002700; Chromosome I.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:UniProtKB-UniRule.
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; Transferase.
FT   CHAIN           1..287
FT                   /note="Pyridoxal kinase PdxY"
FT                   /id="PRO_0000269799"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         44..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
SQ   SEQUENCE   287 AA;  31202 MW;  1DAF47C6235AD2AE CRC64;
     MKNVLSIQSH VIYGHAGNSA AVFPMQRLGV NVWPLNTVQL SNHMQYGHWA GSAIDAAKME
     QLVDGIAAIG ALKRCDAVLS GFLGSPAQAR AAVEIVRTVK ATNPNAWYFC DPAMGQTGGI
     RPEPGVEEFI VAELPELADG MAPNHSELQK LAGQRIETVA EAVAACRLII RRGPQVILVK
     HLHDRNSPAD RFNMLVVTET EAWIGQRPLY AFPRHPVGVG DLTSAIFVAR RLRGDSVRAA
     FEHTLAAVHA VVKATYDARR YELELVAAQD EIARPSEWFG AWVTGAD
 
 
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