ID   PDXY_ECOL5              Reviewed;         287 AA.
AC   Q0THJ1;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=ECP_1581;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage
CC       pathway. Uses pyridoxamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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DR   EMBL; CP000247; ABG69588.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_669489.1; -.
DR   SMR; Q0THJ1; 1-286.
DR   GeneID; 4190463; -.
DR   GenomeReviews; CP000247_GR; ECP_1581.
DR   KEGG; ecp:ECP_1581; -.
DR   HOGENOM; Q0THJ1; -.
DR   BioCyc; ECOL362663:ECP_1581-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004340; F:glucokinase activity; IEA:HAMAP.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01639; -; 1.
DR   InterPro; IPR013749; HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF08543; Phos_pyr_kin; 1.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    287       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269810.
FT   NP_BIND     182    183       ATP (By similarity).
FT   NP_BIND     208    223       ATP (By similarity).
FT   BINDING      10     10       Substrate (By similarity).
FT   BINDING      45     45       Substrate (By similarity).
FT   BINDING     224    224       Substrate (By similarity).
SQ   SEQUENCE   287 AA;  31334 MW;  D8061DBD92CE559A CRC64;
     MMKNILAIQS HVVYGHAGNS AAEFPMRRLG ANVWPLNTVQ FSNHTQYGKW TGCVMPPSHL
     TEIVQGIAAI DKLHTCDAVL SGYLGSAEQG EHILGIVRQV KAANPQAKYF CDPVMGHPEK
     GCIVAPGVAE FHVRHGLPAS DIIAPNLVEL EILCEHPVNN VEEAVLAARE LIAQGPQIVL
     VKHLARAGYS RDRFEMLLVT ADEAWHISRP LVDFGMRQPV GVGDVTSGLL LVKLLQGATL
     QEALEHVTAA VYEIMVTTKA MQEYELQVVA AQDRIANPEH YFSATKL
//