ID   PDXY_SHISS              Reviewed;         287 AA.
AC   Q3Z1Z2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=SSON_1520;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ88220.1; -; Genomic_DNA.
DR   RefSeq; YP_310455.1; -.
DR   SMR; Q3Z1Z2; 1-286.
DR   GeneID; 3667165; -.
DR   GenomeReviews; CP000038_GR; SSON_1520.
DR   KEGG; ssn:SSON_1520; -.
DR   HOGENOM; Q3Z1Z2; -.
DR   OMA; Q3Z1Z2; EVLLETQ.
DR   BioCyc; SSON300269:SSO_1520-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_0000269833.
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;  31350 MW;  CD1316499BDCDFA1 CRC64;
     MMKNILAIQS HVVYGHAGNS AAEFPMRRLG ANVWPLNTVQ FSNHTQYGKW TGCVMPPSHL
     TEIVQGIAAI DKLHTCDAVL SGYLGSAEQG EHILGIVRQV KAANPQAKYF CDPVMGHPEK
     GCIVAPGVAE FHVRHGLPAS DIIAPNLVEL EILCEHAVNN VEEAVLAARE LIAQGPQIVL
     VKHLARAGYS RDRFEMLLVT ADEAWHISRP LVDFGMRQPV GVGDVTSGLL LVKLLQGATL
     QEVLEHVTAA VYEIMVTTKA MQEYELQVVA AQDRIAKPEH YFSATKL
//